ID A0A8H7VN83_9FUNG Unreviewed; 1174 AA.
AC A0A8H7VN83;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 15.
DE RecName: Full=Glycerophosphocholine phosphodiesterase {ECO:0008006|Google:ProtNLM};
GN ORFNames=INT45_010916 {ECO:0000313|EMBL:KAG2220854.1};
OS Circinella minor.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Circinella.
OX NCBI_TaxID=1195481 {ECO:0000313|EMBL:KAG2220854.1, ECO:0000313|Proteomes:UP000646827};
RN [1] {ECO:0000313|EMBL:KAG2220854.1, ECO:0000313|Proteomes:UP000646827}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 142.35 {ECO:0000313|EMBL:KAG2220854.1,
RC ECO:0000313|Proteomes:UP000646827};
RA Muszewska A., Okrasinska A., Steczkiewicz K., Drgas O., Orlowska M.,
RA Perlinska-Lenart U., Aleksandrzak-Piekarczyk T., Szatraj K.,
RA Zielenkiewicz U., Pilsyk S., Malc E., Mieczkowski P., Kruszewska J.S.,
RA Biernat P., Pawlowska J.;
RT "Metabolic potential, ecology and presence of endohyphal bacteria is
RT reflected in genomic diversity of Mucoromycotina.";
RL Submitted (DEC-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAG2220854.1}.
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DR EMBL; JAEPRB010000127; KAG2220854.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8H7VN83; -.
DR OrthoDB; 197419at2759; -.
DR Proteomes; UP000646827; Unassembled WGS sequence.
DR GO; GO:0047389; F:glycerophosphocholine phosphodiesterase activity; IEA:TreeGrafter.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; IEA:TreeGrafter.
DR CDD; cd14484; SPX_GDE1_like; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR057506; C2_GPCPD1.
DR InterPro; IPR051578; GDPD.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR004331; SPX_dom.
DR PANTHER; PTHR22958:SF1; GLYCEROPHOSPHOCHOLINE PHOSPHODIESTERASE GPCPD1; 1.
DR PANTHER; PTHR22958; GLYCEROPHOSPHORYL DIESTER PHOSPHODIESTERASE; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF25329; C2_GDE1; 1.
DR Pfam; PF03009; GDPD; 1.
DR Pfam; PF03105; SPX; 2.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS51704; GP_PDE; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS51382; SPX; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000646827};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..169
FT /note="SPX"
FT /evidence="ECO:0000259|PROSITE:PS51382"
FT REPEAT 352..375
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 455..487
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 488..512
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 523..555
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 800..1165
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
FT REGION 80..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..96
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1174 AA; 130245 MW; E854D26D48F2D7D9 CRC64;
MKFGKTLLRN QIPEWSKNYL NYKSLKKAIK EAARNSPPLE EDTTGNAIEL EKVDTFYTYK
QSQLDRRLWI LSEKYHQYYP TNSQSSSTTT NNNNDDLSSD GEGTLNGNDS STISSLPDIQ
EELVSALQET RAQMSKIMWF AELNTKGFKK ILKKLDKRLG LDTQNIYYQT KVAILPFASH
EHIRTEIDKL NHWISTLAVA DDRSLIRVST MKHPASVSVK LPMPSTVRRH NHLLTDDEME
QCTLAIDQDD STKLEKLLIT SNTLTTVKSK SDADQARYTL LELAVQRNSL RCIEYLIENG
VNPMEHHDIN ERNILHKLCI LVGEARPEQK SSKVLEALLK WLPELPVQKD FAGRRPLHYA
SEFGQSETVR MLMNHAIRYG YYGQEGFTDP AWQDREGHTP LFLSILHGNF QTLSVLIECG
HIKDIDNVIA AASQRNGNGV TNNNDSIPEF ARLSHHPSAV AMACAQSNLE LLNLLIDNGA
KVDLADEDGE TALHIAVRTH FTEGVRALIT RGHANVNLPE KINAWTPLII AAIEGCQDIA
ELLLEAKADK TCKDNDGWKA YEHAVFRGHP DIGRITKPEV DLTNYKFPRP AINGGNSTQG
PSAGSQSPPT KARNRAGRLY GHKYLTDQCM IIVKLGSNDV RNPLSQRFLK IDDSKLDEQR
LSIAISAVNA TGELPILDLP PNNQQSLLHP EPLVLFATKP EDVILRFDLL ETFGLHQSDK
IIARGTATFD TDLIYTKSKG FKGNAAGNSS LRGQHIVPLV KATTLDCIGS LGFEYFVVTP
FTHPKMTVGD RYMYYKSLDT KIIGHRGSGM NKRAARLQVG ENTVLSFITA ASLGAEYVEF
DVQLTKDLVP VIYHDWTVTE TGFDIPLNAI TSEQFLNLRP SGHIREYHTG VSDGTTVDQV
QPDSAIVQQN DTSSSNNNSP IIDTYTGVGG GGGDSTKPSK RLNRSNSLSA IGSPTMYGRA
IATNRLELTR TNKLGKLKGN GPESIQAPFT TLVEALKQIP KSAGCNIEVK YPMIDEAESD
ELYQFQEINI FVDTILKVVY DNAEDDRRII FSSFHPEICV ALNLKQPNYP VFFLTDAGTL
PMADVRCNSI QGAVRFAKQA DLLGIVTASE PILEAPRMTT IIKESGLLLF TYGVLNNEVE
NAVAQKKYGV DAVIVDSVGA VRKGLQGEPQ VTTA
//
